1. Field of the Invention
This invention involves novel antibody catalysts and a process for their production. The process includes selecting a hapten based on its relationship to the structure and reactivity of a selected substrate so that the hapten, upon attachment to a carrier protein and injection into an animal, elicits an immune response in which the desired antibody is produced.
There has been a long felt, and there is at present, an increasing need for more specific or selective catalysts capable of accelerating rates of desired chemical reactions. Catalysts are used widely in the chemical, pharmaceutical and food processing industries to improve normally unfavorable reaction rates. Among known catalysts, enzymes--naturally occurring protein molecules--excel in terms of their ability to select one reactant species among a large excess of others and to generate the highest acceleration of reaction rates concomitant with this selectivity. Simpler catalysts--based on organics or metals, for instance--lack the ability of enzymes to select substrates. The success of enzymes is attributed to the ability of proteins to fold spatially so as to create specific pockets for binding a reactant, and to place catalytically active groups within these pockets in proximity to a reactant. These pockets are referred to as "active sites".
A major obstacle to creating new enzymes which would operate upon a predetermined reactant and selectively catalyze a desired chemical transformation on this species is the understanding of how proteins achieve their spatial folded form. Minor alterations to an enzyme (and its function as a catalyst) are possible, via site-directed alterations in its sequence. However, substitution of a single amino acid for another in the sequence of a protein can affect the conformation and/or function of the molecule in a severe and unpredictable manner.
2. Description of the Prior Art
International Patent PCT/US84/01951; Lerner (Advances in Immunology 36, 1, 1984); Raso and Stollar (Biochemistry 14, 585, 591, 1975); Kohen et al (FEBS Letters 100, 137, 1979; 104, 201, 1979; 111, 427, 1980; and Biochim. Biphys. Acta. 629, 328, 1980); Slobin (Biochemistry 5, 2836, 1966); and G. P. Royer (Advances in Catalysis, 29, 197-227, 1980) are cited as representative of the state of the art.